메뉴 건너뛰기




Volumn 26, Issue 16, 2008, Pages 1942-1954

Identification and characterization of novel antigenic vaccine candidates of Actinobacillus pleuropneumoniae

Author keywords

A. pleuropneumoniae; Outer membrane proteins; Vaccine

Indexed keywords

BACTERIAL ANTIGEN; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; OUTER MEMBRANE PROTEIN COML; OUTER MEMBRANE PROTEIN LOLB; OUTER MEMBRANE PROTEIN LPPC; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 40849117864     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2008.02.022     Document Type: Article
Times cited : (26)

References (69)
  • 1
    • 0033631612 scopus 로고    scopus 로고
    • Experimental aerosol transmission of Actinobacillus pleuropneumoniae to pigs
    • Jobert J.E., Savoye C., Cariolet R., Kobisch M., and Madec F. Experimental aerosol transmission of Actinobacillus pleuropneumoniae to pigs. Can J Vet Res 64 (2000) 21-26
    • (2000) Can J Vet Res , vol.64 , pp. 21-26
    • Jobert, J.E.1    Savoye, C.2    Cariolet, R.3    Kobisch, M.4    Madec, F.5
  • 2
    • 0031204719 scopus 로고    scopus 로고
    • Airborne transmission of Actinobacillus pleuropneumoniae and porcine reproductive and respiratory syndrome virus in nursery pigs
    • Torremorell M., Pijoan C., Janni K., Walker R., and Joo H.S. Airborne transmission of Actinobacillus pleuropneumoniae and porcine reproductive and respiratory syndrome virus in nursery pigs. Am J Vet Res 58 (1997) 828-832
    • (1997) Am J Vet Res , vol.58 , pp. 828-832
    • Torremorell, M.1    Pijoan, C.2    Janni, K.3    Walker, R.4    Joo, H.S.5
  • 5
    • 0038444004 scopus 로고    scopus 로고
    • Association of Actinobacillus pleuropneumoniae capsular polysaccharide with virulence in pigs
    • Bandara A.B., Lawrence M.L., Veit H.P., and Inzana T.J. Association of Actinobacillus pleuropneumoniae capsular polysaccharide with virulence in pigs. Infect Immun 71 (2003) 3320-3328
    • (2003) Infect Immun , vol.71 , pp. 3320-3328
    • Bandara, A.B.1    Lawrence, M.L.2    Veit, H.P.3    Inzana, T.J.4
  • 6
    • 0023721810 scopus 로고
    • Virulence properties and protective efficacy of the capsular polymer of Haemophilus-(Actinobacillus)-pleuropneumoniae serotype-5
    • Inzana T.J., Ma J.N., Workman T., Gogolewski R.P., and Anderson P. Virulence properties and protective efficacy of the capsular polymer of Haemophilus-(Actinobacillus)-pleuropneumoniae serotype-5. Infect Immun 56 (1988) 1880-1889
    • (1988) Infect Immun , vol.56 , pp. 1880-1889
    • Inzana, T.J.1    Ma, J.N.2    Workman, T.3    Gogolewski, R.P.4    Anderson, P.5
  • 7
    • 0037046282 scopus 로고    scopus 로고
    • Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infection
    • Baltes N., Hennig-Pauka I., and Gerlach G.F. Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infection. FEMS Microbiol Lett 209 (2002) 283-287
    • (2002) FEMS Microbiol Lett , vol.209 , pp. 283-287
    • Baltes, N.1    Hennig-Pauka, I.2    Gerlach, G.F.3
  • 8
    • 0035158915 scopus 로고    scopus 로고
    • Actinobacillus pleuropneumoniae iron transport and urease activity: effects on bacterial virulence and host immune response
    • Baltes N., Tonpitak W., Gerlach G.F., Hennig-Pauka I., Hoffmann-Moujahid A., Ganter M., et al. Actinobacillus pleuropneumoniae iron transport and urease activity: effects on bacterial virulence and host immune response. Infect Immun 69 (2001) 472-478
    • (2001) Infect Immun , vol.69 , pp. 472-478
    • Baltes, N.1    Tonpitak, W.2    Gerlach, G.F.3    Hennig-Pauka, I.4    Hoffmann-Moujahid, A.5    Ganter, M.6
  • 9
    • 33745770603 scopus 로고    scopus 로고
    • FhuA and HgbA, outer membrane proteins of Actinobacillus pleuropneumoniae: their role as virulence determinants
    • Shakarji L., Mikael L.G., Srikumar R., Kobisch M., Coulton J.W., and Jacques M. FhuA and HgbA, outer membrane proteins of Actinobacillus pleuropneumoniae: their role as virulence determinants. Can J Microbiol 52 (2006) 391-396
    • (2006) Can J Microbiol , vol.52 , pp. 391-396
    • Shakarji, L.1    Mikael, L.G.2    Srikumar, R.3    Kobisch, M.4    Coulton, J.W.5    Jacques, M.6
  • 10
    • 0028980091 scopus 로고
    • Virulence in Actinobacillus pleuropneumoniae and RTX toxins
    • Frey J. Virulence in Actinobacillus pleuropneumoniae and RTX toxins. Trends Microbiol 3 (1995) 257-261
    • (1995) Trends Microbiol , vol.3 , pp. 257-261
    • Frey, J.1
  • 11
    • 0032841470 scopus 로고    scopus 로고
    • Characterization of apxIVA, a new RTX determinant of Actinobacillus pleuropneumoniae
    • Schaller A., Kuhn R., Kuhnert P., Nicolet J., Anderson T.J., MacInnes J.I., et al. Characterization of apxIVA, a new RTX determinant of Actinobacillus pleuropneumoniae. Microbiology 145 (1999) 2105-2116
    • (1999) Microbiology , vol.145 , pp. 2105-2116
    • Schaller, A.1    Kuhn, R.2    Kuhnert, P.3    Nicolet, J.4    Anderson, T.J.5    MacInnes, J.I.6
  • 12
    • 0025094605 scopus 로고
    • Role of lipopolysaccharides in adherence of Actinobacillus pleuropneumoniae to porcine tracheal rings
    • Bélanger M., Dubreuil D., Harel J., Girard C., and Jacques M. Role of lipopolysaccharides in adherence of Actinobacillus pleuropneumoniae to porcine tracheal rings. Infect Immun 58 (1990) 3523-3530
    • (1990) Infect Immun , vol.58 , pp. 3523-3530
    • Bélanger, M.1    Dubreuil, D.2    Harel, J.3    Girard, C.4    Jacques, M.5
  • 13
    • 28244439062 scopus 로고    scopus 로고
    • Truncation of the lipopolysaccharide outer core affects susceptibility to antimicrobial peptides and virulence of Actinobacillus pleuropneumoniae serotype 1
    • Ramjeet M., Deslandes V., St. Michael F., Cox A.D., Kobisch M., Gottschalk M., et al. Truncation of the lipopolysaccharide outer core affects susceptibility to antimicrobial peptides and virulence of Actinobacillus pleuropneumoniae serotype 1. J Biol Chem 280 (2005) 39104-39114
    • (2005) J Biol Chem , vol.280 , pp. 39104-39114
    • Ramjeet, M.1    Deslandes, V.2    St. Michael, F.3    Cox, A.D.4    Kobisch, M.5    Gottschalk, M.6
  • 14
    • 0034166655 scopus 로고    scopus 로고
    • A 24-kDa cloned zinc metalloprotease from Actinobacillus pleuropneumoniae is common to all serotypes and cleaves actin in vitro
    • Garcia-Cuellar C., Montanez C., Tenorio V., Reyes-Esparza J., Duran M.J., Negrete E., et al. A 24-kDa cloned zinc metalloprotease from Actinobacillus pleuropneumoniae is common to all serotypes and cleaves actin in vitro. Can J Vet Res 64 (2000) 88-95
    • (2000) Can J Vet Res , vol.64 , pp. 88-95
    • Garcia-Cuellar, C.1    Montanez, C.2    Tenorio, V.3    Reyes-Esparza, J.4    Duran, M.J.5    Negrete, E.6
  • 18
    • 0344420187 scopus 로고    scopus 로고
    • Identification of dimethyl sulfoxide reductase in Actinobacillus pleuropneumoniae and its role in infection
    • Baltes N., Hennig-Pauka I., Jacobsen I., Gruber A.D., and Gerlach G.F. Identification of dimethyl sulfoxide reductase in Actinobacillus pleuropneumoniae and its role in infection. Infect Immun 71 (2003) 6784-6792
    • (2003) Infect Immun , vol.71 , pp. 6784-6792
    • Baltes, N.1    Hennig-Pauka, I.2    Jacobsen, I.3    Gruber, A.D.4    Gerlach, G.F.5
  • 19
    • 23344443979 scopus 로고    scopus 로고
    • Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract
    • Baltes N., N'diaye M., Jacobsen I.D., Maas A., Buettner F.F.R., and Gerlach G.F. Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract. Infect Immun 73 (2005) 4614-4619
    • (2005) Infect Immun , vol.73 , pp. 4614-4619
    • Baltes, N.1    N'diaye, M.2    Jacobsen, I.D.3    Maas, A.4    Buettner, F.F.R.5    Gerlach, G.F.6
  • 20
    • 11144305046 scopus 로고    scopus 로고
    • Enzymes involved in anaerobic respiration appear to play a role in Actinobacillus pleuropneumoniae virulence
    • Jacobsen I., Hennig-Pauka I., Baltes N., Trost M., and Gerlach G.F. Enzymes involved in anaerobic respiration appear to play a role in Actinobacillus pleuropneumoniae virulence. Infect Immun 73 (2005) 226-234
    • (2005) Infect Immun , vol.73 , pp. 226-234
    • Jacobsen, I.1    Hennig-Pauka, I.2    Baltes, N.3    Trost, M.4    Gerlach, G.F.5
  • 22
    • 0021455059 scopus 로고
    • Haemophilus pleuropneumoniae serotypes-cross protection experiments
    • Nielsen R. Haemophilus pleuropneumoniae serotypes-cross protection experiments. Nord Vet Med 36 (1984) 221-234
    • (1984) Nord Vet Med , vol.36 , pp. 221-234
    • Nielsen, R.1
  • 23
    • 0029069357 scopus 로고
    • Convalescent pigs are protected completely against infection with a homologous Actinobacillus pleuropneumoniae strain but incompletely against a heterologous-serotype strain
    • Cruijsen T., Vanleengoed L., Hamhoffies M., and Verheijden J.H.M. Convalescent pigs are protected completely against infection with a homologous Actinobacillus pleuropneumoniae strain but incompletely against a heterologous-serotype strain. Infect Immun 63 (1995) 2341-2343
    • (1995) Infect Immun , vol.63 , pp. 2341-2343
    • Cruijsen, T.1    Vanleengoed, L.2    Hamhoffies, M.3    Verheijden, J.H.M.4
  • 24
    • 0030272847 scopus 로고    scopus 로고
    • Cross-protection between Actinobacillus pleuropneumoniae biotypes-serotypes in pigs
    • Haesebrouck F., van de Kerkhof A., Dom P., Chiers K., and Ducatelle R. Cross-protection between Actinobacillus pleuropneumoniae biotypes-serotypes in pigs. Vet Microbiol 52 (1996) 277-284
    • (1996) Vet Microbiol , vol.52 , pp. 277-284
    • Haesebrouck, F.1    van de Kerkhof, A.2    Dom, P.3    Chiers, K.4    Ducatelle, R.5
  • 25
    • 0025649705 scopus 로고
    • Humoral antibody response and protective immunity in swine following immunization with the 104-kilodalton hemolysin of Actinobacillus pleuropneumoniae
    • Devenish J., Rosendal S., and Bossé T.J. Humoral antibody response and protective immunity in swine following immunization with the 104-kilodalton hemolysin of Actinobacillus pleuropneumoniae. Infect Immun 58 (1990) 3829-3832
    • (1990) Infect Immun , vol.58 , pp. 3829-3832
    • Devenish, J.1    Rosendal, S.2    Bossé, T.J.3
  • 26
    • 0031766779 scopus 로고    scopus 로고
    • Evaluation of the protective efficacy of Actinobacillus pleuropneumoniae serotype 1 detoxified lipopolysaccharides or O-polysaccharide-protein conjugate in pigs
    • Rioux S., Girard C., Dubreuil J.D., and Jacques M. Evaluation of the protective efficacy of Actinobacillus pleuropneumoniae serotype 1 detoxified lipopolysaccharides or O-polysaccharide-protein conjugate in pigs. Res Vet Sci 65 (1998) 165-167
    • (1998) Res Vet Sci , vol.65 , pp. 165-167
    • Rioux, S.1    Girard, C.2    Dubreuil, J.D.3    Jacques, M.4
  • 27
    • 0027446412 scopus 로고
    • Molecular characterization of a protective outer membrane lipoprotein (OmlA) from Actinobacillus pleuropneumoniae serotype 1
    • Gerlach G.F., Anderson C., Klashinsky S., Rossi-Campos A., Potter A.A., and Willson P.J. Molecular characterization of a protective outer membrane lipoprotein (OmlA) from Actinobacillus pleuropneumoniae serotype 1. Infect Immun 61 (1993) 565-572
    • (1993) Infect Immun , vol.61 , pp. 565-572
    • Gerlach, G.F.1    Anderson, C.2    Klashinsky, S.3    Rossi-Campos, A.4    Potter, A.A.5    Willson, P.J.6
  • 28
    • 0026734528 scopus 로고
    • Immunization of pigs against Actinobacillus pleuropneumoniae with two recombinant protein preparations
    • Rossi-Campos A., Anderson C., Gerlach G.F., Klashinsky S., Potter A.A., and Willson P.J. Immunization of pigs against Actinobacillus pleuropneumoniae with two recombinant protein preparations. Vaccine 10 (1992) 512-518
    • (1992) Vaccine , vol.10 , pp. 512-518
    • Rossi-Campos, A.1    Anderson, C.2    Gerlach, G.F.3    Klashinsky, S.4    Potter, A.A.5    Willson, P.J.6
  • 29
    • 17944363598 scopus 로고    scopus 로고
    • An evaluation of the role of antibodies to Actinobacillus pleuropneumoniae serovar 1 and 15 in the protection provided by sub-unit and live streptomycin-dependent pleuropneumonia vaccines
    • Tumamao J.Q., Bowles R.E., van den Bosch H., Klaasen H.L., Fenwick B.W., and Blackall P.J. An evaluation of the role of antibodies to Actinobacillus pleuropneumoniae serovar 1 and 15 in the protection provided by sub-unit and live streptomycin-dependent pleuropneumonia vaccines. Aust Vet J 82 (2004) 773-780
    • (2004) Aust Vet J , vol.82 , pp. 773-780
    • Tumamao, J.Q.1    Bowles, R.E.2    van den Bosch, H.3    Klaasen, H.L.4    Fenwick, B.W.5    Blackall, P.J.6
  • 30
    • 3342964506 scopus 로고    scopus 로고
    • Comparison of the efficacy of a subunit and a live streptomycin-dependent porcine pleuropneumonia vaccine
    • Tumamao J.Q., Bowles R.E., van den Bosch H., Klaasen H.L., Fenwick B.W., Storie G.J., et al. Comparison of the efficacy of a subunit and a live streptomycin-dependent porcine pleuropneumonia vaccine. Aust Vet J 82 (2004) 370-374
    • (2004) Aust Vet J , vol.82 , pp. 370-374
    • Tumamao, J.Q.1    Bowles, R.E.2    van den Bosch, H.3    Klaasen, H.L.4    Fenwick, B.W.5    Storie, G.J.6
  • 32
    • 0034887533 scopus 로고    scopus 로고
    • Identification and characterization of App: an immunogenic autotransporter protein of Neisseria meningitidis
    • Hadi H.A., Wooldridge K.G., Robinson K., and Ala'Aldeen D.A.A. Identification and characterization of App: an immunogenic autotransporter protein of Neisseria meningitidis. Mol Micro 41 (2001) 611-623
    • (2001) Mol Micro , vol.41 , pp. 611-623
    • Hadi, H.A.1    Wooldridge, K.G.2    Robinson, K.3    Ala'Aldeen, D.A.A.4
  • 33
    • 0033042694 scopus 로고    scopus 로고
    • Identification and characterization of TspA, a major CD4+ T-Cell- and B-Cell-stimulating Neisseria-specific antigen
    • Kizil G., Todd I., Atta M., Borriello S.P., Ait-Tahar K., and Ala'Aldeen D.A.A. Identification and characterization of TspA, a major CD4+ T-Cell- and B-Cell-stimulating Neisseria-specific antigen. Infect Immun 67 (1999) 3533-3541
    • (1999) Infect Immun , vol.67 , pp. 3533-3541
    • Kizil, G.1    Todd, I.2    Atta, M.3    Borriello, S.P.4    Ait-Tahar, K.5    Ala'Aldeen, D.A.A.6
  • 35
    • 1842582680 scopus 로고    scopus 로고
    • Harnessing natural transformation in Actinobacillus pleuropneumoniae: a simple method for allelic replacements
    • Bossé J.T., Nash J.H.E., Kroll S.J., and Langford P.R. Harnessing natural transformation in Actinobacillus pleuropneumoniae: a simple method for allelic replacements. FEMS Microbiol Lett 233 (2004) 277-281
    • (2004) FEMS Microbiol Lett , vol.233 , pp. 277-281
    • Bossé, J.T.1    Nash, J.H.E.2    Kroll, S.J.3    Langford, P.R.4
  • 36
    • 33947407705 scopus 로고    scopus 로고
    • CapA, an autotransporter protein of Campylobacter jejuni, mediates association to human epithelial cells and colonization of the chicken gut
    • Ashgar S.S.A., Oldfield N.J., Wooldridge K.G., Jones M.A., Irving G.J., Turner D.P.J., et al. CapA, an autotransporter protein of Campylobacter jejuni, mediates association to human epithelial cells and colonization of the chicken gut. J Bacteriol 189 (2006) 1856-1865
    • (2006) J Bacteriol , vol.189 , pp. 1856-1865
    • Ashgar, S.S.A.1    Oldfield, N.J.2    Wooldridge, K.G.3    Jones, M.A.4    Irving, G.J.5    Turner, D.P.J.6
  • 37
    • 0020316141 scopus 로고
    • Tylosin tartrate and tiamutilin effects on experimental piglet pneumonia induced with pneumonic pig lung homogenate containing mycoplasmas, bacteria and viruses
    • Hannan P.C., Bhogal B.S., and Fish J.P. Tylosin tartrate and tiamutilin effects on experimental piglet pneumonia induced with pneumonic pig lung homogenate containing mycoplasmas, bacteria and viruses. Res Vet Sci 33 (1982) 76-88
    • (1982) Res Vet Sci , vol.33 , pp. 76-88
    • Hannan, P.C.1    Bhogal, B.S.2    Fish, J.P.3
  • 38
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy J.L., Laird M.R., Chen F., Rey S., Walsh C.J., Ester M., et al. PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21 (2005) 617-623
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6
  • 40
    • 0029867376 scopus 로고    scopus 로고
    • A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae
    • Fussenegger M., Facius D., Meier J., and Meyer T.F. A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae. Mol Microbiol 19 (1996) 1095-1105
    • (1996) Mol Microbiol , vol.19 , pp. 1095-1105
    • Fussenegger, M.1    Facius, D.2    Meier, J.3    Meyer, T.F.4
  • 41
    • 5044220423 scopus 로고    scopus 로고
    • The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens
    • Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., et al. The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens. Nat Biotech 22 (2004) 1275-1281
    • (2004) Nat Biotech , vol.22 , pp. 1275-1281
    • Hong, S.H.1    Kim, J.S.2    Lee, S.Y.3    In, Y.H.4    Choi, S.S.5    Rih, J.-K.6
  • 42
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama S.-I., Yokota N., and Tokuda H. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J 16 (1997) 6947-6955
    • (1997) EMBO J , vol.16 , pp. 6947-6955
    • Matsuyama, S.-I.1    Yokota, N.2    Tokuda, H.3
  • 43
    • 0034750231 scopus 로고    scopus 로고
    • Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm
    • Tanaka K., Matsuyama S.-I., and Tokuda H. Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm. J Bacteriol 183 22 (2001) 6538-6542
    • (2001) J Bacteriol , vol.183 , Issue.22 , pp. 6538-6542
    • Tanaka, K.1    Matsuyama, S.-I.2    Tokuda, H.3
  • 44
    • 0030217835 scopus 로고    scopus 로고
    • The isolation of recombinant plasmids expressing secreted antigens of Pasteurella haemolytica A1 and the characterization of an immunogenic 60 kDa antigen
    • Lo R.Y.C., and Mellors A. The isolation of recombinant plasmids expressing secreted antigens of Pasteurella haemolytica A1 and the characterization of an immunogenic 60 kDa antigen. Vet Microbiol 51 (1996) 381-391
    • (1996) Vet Microbiol , vol.51 , pp. 381-391
    • Lo, R.Y.C.1    Mellors, A.2
  • 45
    • 4344580280 scopus 로고    scopus 로고
    • Sequence diversity and molecular evolution of the heat-modifiable outer membrane protein gene (ompA) of Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi
    • Davies R.L., and Lee I. Sequence diversity and molecular evolution of the heat-modifiable outer membrane protein gene (ompA) of Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi. J Bacteriol 186 (2004) 5741-5752
    • (2004) J Bacteriol , vol.186 , pp. 5741-5752
    • Davies, R.L.1    Lee, I.2
  • 46
    • 0031032317 scopus 로고    scopus 로고
    • Purification and partial characterization of the OmpA family of proteins of Pasteurella haemolytica
    • Mahasreshti P., Murphy G., Wyckoff III J., Farmer S., Hancock R., and Confer A. Purification and partial characterization of the OmpA family of proteins of Pasteurella haemolytica. Infect Immun 65 (1997) 211-218
    • (1997) Infect Immun , vol.65 , pp. 211-218
    • Mahasreshti, P.1    Murphy, G.2    Wyckoff III, J.3    Farmer, S.4    Hancock, R.5    Confer, A.6
  • 47
    • 0032794169 scopus 로고    scopus 로고
    • Molecular cloning of the Pasteurella haemolytica pomA gene and identification of bovine antibodies against PomA surface domains
    • Zeng H., Pandher K., and Murphy G.L. Molecular cloning of the Pasteurella haemolytica pomA gene and identification of bovine antibodies against PomA surface domains. Infect Immun 67 (1999) 4968-4973
    • (1999) Infect Immun , vol.67 , pp. 4968-4973
    • Zeng, H.1    Pandher, K.2    Murphy, G.L.3
  • 48
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora A., Abildgaard F., Bushweller J.H., and Tamm L.K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat Struct Mol Biol 8 (2001) 334-338
    • (2001) Nat Struct Mol Biol , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 49
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot R., and Vanderleyden J. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol Microbiol 12 (1994) 333-334
    • (1994) Mol Microbiol , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 50
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag I., Schwarz H., Hirota Y., and Henning U. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol 136 (1978) 280-285
    • (1978) J Bacteriol , vol.136 , pp. 280-285
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3    Henning, U.4
  • 51
    • 0041976985 scopus 로고    scopus 로고
    • Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: evidence of its role in P. multocida interaction with extracellular matrix molecules
    • Dabo S.M., Confer A.W., and Quijano-Blas R.A. Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: evidence of its role in P. multocida interaction with extracellular matrix molecules. Microb Pathog 35 (2003) 147-157
    • (2003) Microb Pathog , vol.35 , pp. 147-157
    • Dabo, S.M.1    Confer, A.W.2    Quijano-Blas, R.A.3
  • 52
    • 0023642579 scopus 로고
    • A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K-12
    • Ried G., and Henning U. A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K-12. FEBS Lett 223 (1987) 387-390
    • (1987) FEBS Lett , vol.223 , pp. 387-390
    • Ried, G.1    Henning, U.2
  • 53
    • 0028064471 scopus 로고
    • Identification of an immunoglobulin Fc receptor of Actinobacillus actinomycetemcomitans
    • Mintz K.P., and Fives-Taylor P.M. Identification of an immunoglobulin Fc receptor of Actinobacillus actinomycetemcomitans. Infect Immun 62 (1994) 4500-4505
    • (1994) Infect Immun , vol.62 , pp. 4500-4505
    • Mintz, K.P.1    Fives-Taylor, P.M.2
  • 54
    • 0022358531 scopus 로고
    • Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12
    • Morona R., Krämer C., and Henning U. Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12. J Bacteriol 164 (1985) 539-543
    • (1985) J Bacteriol , vol.164 , pp. 539-543
    • Morona, R.1    Krämer, C.2    Henning, U.3
  • 55
    • 0015812584 scopus 로고
    • Characterization of Escherichia coli mutants tolerant to bacteriocin JF246: two new classes of tolerant mutants
    • Foulds J., and Barrett C. Characterization of Escherichia coli mutants tolerant to bacteriocin JF246: two new classes of tolerant mutants. J Bacteriol 116 (1973) 885-892
    • (1973) J Bacteriol , vol.116 , pp. 885-892
    • Foulds, J.1    Barrett, C.2
  • 56
    • 0242668756 scopus 로고    scopus 로고
    • fhuA of Actinobacillus pleuropneumoniae encodes a ferrichrome receptor but is not regulated by iron
    • Mikael L.G., Srikumar R., Coulton J.W., and Jacques M. fhuA of Actinobacillus pleuropneumoniae encodes a ferrichrome receptor but is not regulated by iron. Infect Immun 71 (2003) 2911-2915
    • (2003) Infect Immun , vol.71 , pp. 2911-2915
    • Mikael, L.G.1    Srikumar, R.2    Coulton, J.W.3    Jacques, M.4
  • 57
    • 34250303965 scopus 로고    scopus 로고
    • Outer membrane proteome of Actinobacillus pleuropneumoniae: LC-MS/MS analyses validate in silico predictions
    • Chung J.W., Ng-Thow-Hing C., Budman L.I., Gibbs B.F., Nash J.H.E., Jacques M., et al. Outer membrane proteome of Actinobacillus pleuropneumoniae: LC-MS/MS analyses validate in silico predictions. Proteomics 7 (2007) 1854-1865
    • (2007) Proteomics , vol.7 , pp. 1854-1865
    • Chung, J.W.1    Ng-Thow-Hing, C.2    Budman, L.I.3    Gibbs, B.F.4    Nash, J.H.E.5    Jacques, M.6
  • 58
    • 0031457849 scopus 로고    scopus 로고
    • Actinobacillus pleuropneumoniae infections in pigs: the role of virulence factors in pathogenesis and protection
    • Haesebrouck F., Chiers K., Van Overbeke I., and Ducatelle R. Actinobacillus pleuropneumoniae infections in pigs: the role of virulence factors in pathogenesis and protection. Vet Microbiol 58 (1997) 239-249
    • (1997) Vet Microbiol , vol.58 , pp. 239-249
    • Haesebrouck, F.1    Chiers, K.2    Van Overbeke, I.3    Ducatelle, R.4
  • 59
    • 40849124748 scopus 로고
    • Characterization of comE, a late competence operon of Bacillus subtilis required for the binding and uptake of transforming DNA
    • Hahn J., Inamine G., Kozlov Y., and Dubnau D. Characterization of comE, a late competence operon of Bacillus subtilis required for the binding and uptake of transforming DNA. Mol Microbiol 71 (1993) 5427-5431
    • (1993) Mol Microbiol , vol.71 , pp. 5427-5431
    • Hahn, J.1    Inamine, G.2    Kozlov, Y.3    Dubnau, D.4
  • 60
    • 0029016409 scopus 로고
    • Cloning and characterization of a protective outer membrane lipoprotein of Actinobacillus pleuropneumoniae serotype-5
    • Bunka S., Christensen C., Potter A.A., Willson P.J., and Gerlach G.F. Cloning and characterization of a protective outer membrane lipoprotein of Actinobacillus pleuropneumoniae serotype-5. Infect Immun 63 (1995) 2797-2800
    • (1995) Infect Immun , vol.63 , pp. 2797-2800
    • Bunka, S.1    Christensen, C.2    Potter, A.A.3    Willson, P.J.4    Gerlach, G.F.5
  • 61
    • 0028964621 scopus 로고
    • Molecular cloning of an Actinobacillus pleuropneumoniae outer membrane lipoprotein (OmlA) from serotype 5a
    • Ito H., Uchida I., Sekizaki T., Ooishi E., Kawai T., Okabe T., et al. Molecular cloning of an Actinobacillus pleuropneumoniae outer membrane lipoprotein (OmlA) from serotype 5a. Microb Pathog 18 (1995) 29-36
    • (1995) Microb Pathog , vol.18 , pp. 29-36
    • Ito, H.1    Uchida, I.2    Sekizaki, T.3    Ooishi, E.4    Kawai, T.5    Okabe, T.6
  • 62
    • 0031727232 scopus 로고    scopus 로고
    • Demonstration of the third antigenically distinct outer membrane lipoprotein (OmlA) in Actinobacillus pleuropneumoniae serotype 7
    • Ito H., Osaki M., Uchida I., Ohya T., and Sekizaki T. Demonstration of the third antigenically distinct outer membrane lipoprotein (OmlA) in Actinobacillus pleuropneumoniae serotype 7. FEMS Microbiol Lett 167 (1998) 303-308
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 303-308
    • Ito, H.1    Osaki, M.2    Uchida, I.3    Ohya, T.4    Sekizaki, T.5
  • 63
    • 0033813409 scopus 로고    scopus 로고
    • Identification of Actinobacillus pleuropneumoniae virulence genes using signature tagged mutagenesis in a swine infection model
    • Fuller T.E., Martin S., Teel J.F., Alaniz G.R., Kennedy M.J., and Lowery D.E. Identification of Actinobacillus pleuropneumoniae virulence genes using signature tagged mutagenesis in a swine infection model. Microbiol Pathog 29 (2000) 39-51
    • (2000) Microbiol Pathog , vol.29 , pp. 39-51
    • Fuller, T.E.1    Martin, S.2    Teel, J.F.3    Alaniz, G.R.4    Kennedy, M.J.5    Lowery, D.E.6
  • 64
    • 25444511780 scopus 로고    scopus 로고
    • Identification of Actinobacillus suis genes essential for the colonization of the upper respiratory tract of swine
    • Ojha S., Sirois M., and Macinnes J.I. Identification of Actinobacillus suis genes essential for the colonization of the upper respiratory tract of swine. Infect Immun 73 (2005) 7032-7039
    • (2005) Infect Immun , vol.73 , pp. 7032-7039
    • Ojha, S.1    Sirois, M.2    Macinnes, J.I.3
  • 65
    • 7044286507 scopus 로고    scopus 로고
    • Identification of genes transcribed by Actinobacillus pleuropneumoniae in necrotic porcine lung tissue by using selective capture of transcribed sequences
    • Baltes N., and Gerlach G.F. Identification of genes transcribed by Actinobacillus pleuropneumoniae in necrotic porcine lung tissue by using selective capture of transcribed sequences. Infect Immun 72 (2004) 6711-6716
    • (2004) Infect Immun , vol.72 , pp. 6711-6716
    • Baltes, N.1    Gerlach, G.F.2
  • 66
    • 0027984987 scopus 로고
    • Identification of a potentially important antigen of Pasteurella haemolytica
    • Weldon S.K., Mosier D.A., Simons K.R., Craven R.C., and Confer A.W. Identification of a potentially important antigen of Pasteurella haemolytica. Vet Microbiol 40 (1994) 283-291
    • (1994) Vet Microbiol , vol.40 , pp. 283-291
    • Weldon, S.K.1    Mosier, D.A.2    Simons, K.R.3    Craven, R.C.4    Confer, A.W.5
  • 67
    • 0242286023 scopus 로고    scopus 로고
    • Interference of outer membrane protein PalA with protective immunity against Actinobacillus pleuropneumoniae infections in vaccinated pigs
    • van den Bosch H., and Frey J. Interference of outer membrane protein PalA with protective immunity against Actinobacillus pleuropneumoniae infections in vaccinated pigs. Vaccine 21 (2003) 3601-3607
    • (2003) Vaccine , vol.21 , pp. 3601-3607
    • van den Bosch, H.1    Frey, J.2
  • 68
    • 0026735914 scopus 로고
    • Molecular cloning and expression of ptxA, the gene encoding the 120-Kilodalton cytotoxin of Actinobacillus pleuropneumoniae
    • Macdonald J., and Rycroft A.N. Molecular cloning and expression of ptxA, the gene encoding the 120-Kilodalton cytotoxin of Actinobacillus pleuropneumoniae. Infect Immun 60 (1992) 2726-2732
    • (1992) Infect Immun , vol.60 , pp. 2726-2732
    • Macdonald, J.1    Rycroft, A.N.2
  • 69
    • 0031027838 scopus 로고    scopus 로고
    • Serological characterization of Actinobacillus pleuropneumoniae biotype 2 strains isolated from pigs in two Danish herds
    • Nielsen R., Andresen L.O., Plambeck T., Nielsen J.P., Krarup L.T., and Jorsal S.E. Serological characterization of Actinobacillus pleuropneumoniae biotype 2 strains isolated from pigs in two Danish herds. Vet Microbiol 54 (1997) 35-46
    • (1997) Vet Microbiol , vol.54 , pp. 35-46
    • Nielsen, R.1    Andresen, L.O.2    Plambeck, T.3    Nielsen, J.P.4    Krarup, L.T.5    Jorsal, S.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.